On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171.

ABSTRACT: The structure of two Thermotoga maritima proteins, a conserved hypothetical protein (TM0160) and a transcriptional regulator (TM1171), have now been determined at 1.9 A and 2.3 A resolution, respectively, as part of a large-scale structural genomics project. Our first efforts to crystallize full-length versions of these targets were unsuccessful. However, analysis of the recombinant purified proteins using the technique of enhanced amide hydrogen/deuterium exchange mass spectroscopy (DXMS) revealed substantial regions of rapid amide deuterium hydrogen exchange, consistent with flexible regions of the structures. Based on these exchange data, truncations were designed to selectively remove the disordered C-terminal regions, and the resulting daughter proteins showed greatly enhanced crystal

SUBMITTER: Spraggon G 

PROVIDER: S-EPMC2287321 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature